Crystal structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains (open access)

Crystal structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains

The GntR superfamily of dimeric transcription factors, with more than 6200 members encoded in bacterial genomes, are characterized by N-terminal winged helix (WH) DNA-binding domains and diverse C-terminal, regulatory domains, which provide a basis for the classification of the constituent families. The largest of these families, FadR, contains nearly 3000 proteins with all a-helical regulatory domains classified into two related Pfam families: FadR{_}C and FCD. Only two crystal structures of the FadR family members, i.e. the E. coli FadR protein and the LldR from C. glutamicum, have been described to date in literature. Here we describe the crystal structure of TM0439, a GntR regulator with an FCD domain, found in the Thermotoga maritima genome. The FCD domain is similar to that of the LldR regulator, and contains a buried metal binding site. Using atomic absorption spectroscopy and Trp fluorescence, we show that the recombinant protein contains bound Ni{sup 2+} ions, but it is able to bind Zn{sup 2+} with K{sub D} < 70 nM . We conclude that Zn{sup 2+} is the likely physiological metal, where it may perform either or both structural and regulatory roles. Finally, we compare the TM0439 structure to two other FadR family structures recently deposited …
Date: June 6, 2009
Creator: Zheng, Meiying; Cooper, David; Grossoehmerb, Nickolas; Yu, Minmin; Hung, Li-Wei; Cieslik, Murcin et al.
Object Type: Article
System: The UNT Digital Library
Determining the DUF55-domain structure of human thymocyte nuclear protein 1 from crystals partially twinned by tetartohedry (open access)

Determining the DUF55-domain structure of human thymocyte nuclear protein 1 from crystals partially twinned by tetartohedry

Human thymocyte nuclear protein 1 (hTHYN1) contains a unique DUF55 domain of 167 residues (55-221), but its cellular function is unclear. Crystals of DUF55 belong to the trigonal space group P3{sub 1}, but twinning causes the data to approach an apparent 622 symmetry. Two datasets to 2.3 {angstrom} resolution were collected. Statistical analysis confirmed that both datasets were partially twinned by tetartohedry. Tetartohedral twin fractions were estimated. After the structure was determined, only one twofold axis of rotational pseudosymmetry was found in the crystal structure. Using the DALI program, a YTH domain, which is a potential RNA binding domain from human YTH domain-containing protein 2, was identified to have the most similar three-dimensional fold to DUF55. It is implied that DUF55 might be a potential RNA-related domain.
Date: June 6, 2009
Creator: Yu, Feng; Song, Aixin; Xu, Chunyan; Sun, Lihua; Li, Jian; Tang, Lin et al.
Object Type: Article
System: The UNT Digital Library
Pyramid Lake Reneweable Energy Plan (open access)

Pyramid Lake Reneweable Energy Plan

The Pyramid Lake Renewable Energy Plan covers these areas: energy potential (primarily focusing on geothermal resource potential, but also more generally addressing wind energy potential); renewable energy market potential; transmission system development; geothermal direct use potential; and business structures to accomplish the development objectives of the Pyramid Lake Paiute Tribe.
Date: June 6, 2009
Creator: High Desert Geoculture, LLC
Object Type: Report
System: The UNT Digital Library
A THERMODYNAMIC ANALYSIS OF THE SO2/H2SO4 SYSTEM IN SO2-DEPOLARIZED ELECTROLYSIS (open access)

A THERMODYNAMIC ANALYSIS OF THE SO2/H2SO4 SYSTEM IN SO2-DEPOLARIZED ELECTROLYSIS

None
Date: June 6, 2009
Creator: Gorensek, M.; Staser, J.; Stanford, T. & Weidner, J.
Object Type: Article
System: The UNT Digital Library